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The C-propeptide domains of the fibrillar procollagens, which are present throughout the Metazoa in the form of ∼90 kDa trimers, play crucial roles in both intracellular molecular assembly and extracellular formation of collagen fibrils. The first crystallization of a C-propeptide domain, that from human procollagen III, is described. Following transient expression in mammalian 293T cells of both the native protein and a selenomethionine derivative, two crystal forms of the homotrimer were obtained: an orthorhombic form (P2 12121) that diffracted to 1.7 Å resolution and a trigonal form (P321) that diffracted to 3.5 Å resolution. Characterization by MALDI-TOF mass spectrometry allowed the efficiency of selenomethionine incorporation to be determined. © 2012 International Union of Crystallography.

Original publication

DOI

10.1107/S1744309112035294

Type

Journal article

Journal

Acta Crystallographica Section F: Structural Biology and Crystallization Communications

Publication Date

01/10/2012

Volume

68

Pages

1209 - 1213